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Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
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PDHA1 / PDH E1 Alpha
pyruvate dehydrogenase (lipoamide) alpha 1
The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. The PDH complex is composed of multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 enzyme is a heterotetramer of two alpha and two beta subunits. This gene encodes the E1 alpha 1 subunit containing the E1 active site, and plays a key role in the function of the PDH complex. Mutations in this gene are associated with pyruvate dehydrogenase E1-alpha deficiency and X-linked Leigh syndrome. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells. McFate T, Mohyeldin A, Lu H, Thakar J, Henriques J, Halim ND, Wu H, Schell MJ, Tsang TM, Teahan O, Zhou S, Califano JA, Jeoung NH, Harris RA, Verma A. The Journal of biological chemistry. 2008 283:22700-8.
[PubMed:18541534]
[PMC:PMC2504897]
2
Control of oxidative phosphorylation by vitamin A illuminates a fundamental role in mitochondrial energy homoeostasis. Acin-Perez R, Hoyos B, Zhao F, Vinogradov V, Fischman DA, Harris RA, Leitges M, Wongsiriroj N, Blaner WS, Manfredi G, Hammerling U. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2010 24:627-36.
[PubMed:19812372]
[PMC:PMC2812036]
3
Regulation of intermediary metabolism by the PKCdelta signalosome in mitochondria. Acin-Perez R, Hoyos B, Gong J, Vinogradov V, Fischman DA, Leitges M, Borhan B, Starkov A, Manfredi G, Hammerling U. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2010 24:5033-42. (WB; Mouse)
[PubMed:20798245]
[PMC:PMC2992363]
4
Erk regulation of pyruvate dehydrogenase flux through PDK4 modulates cell proliferation. Grassian AR, Metallo CM, Coloff JL, Stephanopoulos G, Brugge JS. Genes & development. 2011 25:1716-33.
[PubMed:21852536]
[PMC:PMC3165936]
5
p53 negatively regulates transcription of the pyruvate dehydrogenase kinase Pdk2. Contractor T, Harris CR. Cancer research. 2012 72:560-7.
[PubMed:22123926]
6
Two protein kinase C isoforms, and , regulate energy homeostasis in mitochondria by transmitting opposing signals to the pyruvate dehydrogenase complex. Gong J, Hoyos B, Acin-Perez R, Vinogradov V, Shabrova E, Zhao F, Leitges M, Fischman D, Manfredi G, Hammerling U. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2012 26:3537-49. (WB; Mouse)
[PubMed:22573912]
[PMC:PMC3405274]
7
The novel function of tumor protein D54 in regulating pyruvate dehydrogenase and metformin cytotoxicity in breast cancer. Zhuang Y, Ly RC, Frazier CV, Yu J, Qin S, Fan XY, Goetz MP, Boughey JC, Weinshilboum R, Wang L. Cancer & metabolism. 2019 January;7:1. [Full Text Article]
[PubMed:30697423]
[PMC:PMC6345044]
8
Pyruvate dehydrogenase alpha 1 as a target of omega-3 polyunsaturated fatty acids in human prostate cancer through a global phosphoproteomic analysis. Heng Zhao, Beth R Pflug, Xianyin Lai, Mu Wang. Proteomics. 2016 September;16:2419-31. [Full Text Article]
[PubMed:27357730]
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For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.
The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).